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The Drosophila RAD21 cohesin persists at the centromere region in mitosis

Title
The Drosophila RAD21 cohesin persists at the centromere region in mitosis
Type
Article in International Scientific Journal
Year
2000
Authors
Warren, WD
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Steffensen, S
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Lin, E
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Coelho, P
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Loupart, ML
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Cobbe, N
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Lee, JY
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McKay, MJ
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Orr Weaver, T
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Heck, MMS
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Sunkel, CE
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Journal
Title: Current BiologyImported from Authenticus Search for Journal Publications
Vol. 10
Pages: 1463-1466
ISSN: 0960-9822
Publisher: Elsevier
Other information
Authenticus ID: P-000-YG1
Abstract (EN): 'Cohesin' is a highly conserved multiprotein complex thought to be the primary effector of sister-chromatid cohesion in all eukaryotes. Cohesin complexes in budding yeast hold sister chromatids together from S phase until anaphase, but in metazoans, cohesin proteins dissociate from chromosomes and redistribute into the whole cell volume during prophase, well before sister chromatids separate (reviewed in [1,2]). Here we address this apparent anomaly by investigating the cell-cycle dynamics of DRAD21, the Drosophila orthologue of the Xenopus XRAD21 and Saccharomyces cerevisiae Scc1p/Mcd1p cohesins [3]. Analysis of DRAD21 in S2 Drosophila tissue culture cells and live embryos expressing a DRAD21-green fluorescent protein (GFP) fusion revealed the presence of four distinct subcellular pools of DRAD21: a cytoplasmic pool; a chromosome-associated pool which dissociates from chromatin as chromosomes condense in prophase; a short-lived centrosome-associated pool present during meta phase-ana phase; and a centromere-proximal pool which remains bound to condensed chromosomes, is found along the junction of sister chromatids between kinetochores, and persists until the meta phase-anaphase transition. We conclude that in Drosophila, and possibly all metazoans, a minor pool of cohesin remains bound to centromere-proximal chromatin after prophase and maintains sister-chromatid cohesion until the meta ph ase-anaphase transition.
Language: English
Type (Professor's evaluation): Scientific
No. of pages: 4
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